Preliminary experiments in our laboratories have suggested a theoretical basis for the observation of polarization properties dependent on laser frequency in heme protein resonance Raman spectra. The principal objective of this proposal is to test the accuracy of this theory and its implications for determining the local structure of the heme group in solution. The frequency dependence of both linearly and circularly polarized scattering will be measured, using tunable laser frequencies in the range of the alpha and beta transitions. The systems proposed for study are: ferrocytochrome C, hemoglobin, and the heme compound closest to D4h symmetry (alpha, beta, gamma, delta - tetraphenyl porphinatodichlorotin (IV)). We will also attempt to measure Polarized spectra for crystals which have been provided to us for cytochrome C and the D4h model compound. The effect of electronic mixing on the spectra will be investigated using magnetic circular polarization. These data will be used in a normal coordinate analysis, starting with X-ray crystalline structural information and other constraints, to attempt to deduce the structural changes occurring at the heme group in solution.